Header list of 1x59.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 15-MAY-05 1X59
TITLE SOLUTION STRUCTURES OF THE WHEP-TRS DOMAIN OF HUMAN HISTIDYL-TRNA
TITLE 2 SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: WHEP-TRS DOMAIN;
COMPND 5 SYNONYM: HISTIDINE--TRNA LIGASE, HISRS;
COMPND 6 EC: 6.1.1.21;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HARS;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041108-12;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS HISRS, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.NAMEKI,A.SASAGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X59 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X59 1 VERSN
REVDAT 1 15-NOV-05 1X59 0
JRNL AUTH N.NAMEKI,A.SASAGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE WHEP-TRS DOMAIN OF HUMAN
JRNL TITL 2 HISTIDYL-TRNA SYNTHETASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, OPALP 1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), KORADI, R.,BILLETER, M.,GUNTERT,
REMARK 3 P. (OPALP)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X59 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024395.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.85MM WHEP-TRS DOMAIN U
REMARK 210 -15N,13C; 20MM D-TRIS-HCL(PH 7.0)
REMARK 210 ; 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 1.0.7
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 LYS A 58 154.71 63.61
REMARK 500 1 LYS A 60 -69.03 -144.16
REMARK 500 1 SER A 71 -152.74 -85.27
REMARK 500 2 ASP A 55 -69.00 46.66
REMARK 500 2 PHE A 61 -11.30 -143.88
REMARK 500 2 LYS A 64 5.57 -68.54
REMARK 500 2 SER A 68 95.20 -19.90
REMARK 500 2 SER A 71 -50.76 -154.84
REMARK 500 3 SER A 2 58.55 -153.62
REMARK 500 3 SER A 5 58.06 35.68
REMARK 500 3 GLN A 59 -168.10 53.92
REMARK 500 3 PRO A 70 21.08 -73.16
REMARK 500 4 SER A 2 174.30 62.86
REMARK 500 4 PRO A 54 -170.90 -69.94
REMARK 500 4 GLU A 56 140.56 65.24
REMARK 500 4 SER A 57 59.89 34.13
REMARK 500 4 LYS A 58 117.10 -38.20
REMARK 500 4 VAL A 62 58.81 -146.79
REMARK 500 4 LEU A 63 -175.95 57.62
REMARK 500 5 SER A 3 -76.39 -67.74
REMARK 500 5 SER A 5 -26.64 -154.55
REMARK 500 5 SER A 6 -75.48 -71.77
REMARK 500 5 GLN A 31 4.82 -68.46
REMARK 500 5 GLU A 56 75.08 -155.09
REMARK 500 5 GLN A 59 -79.92 64.48
REMARK 500 5 VAL A 62 80.63 -161.85
REMARK 500 5 LEU A 63 -45.77 -133.51
REMARK 500 5 LYS A 64 82.37 49.69
REMARK 500 5 PRO A 70 35.09 -80.56
REMARK 500 5 SER A 71 120.81 65.85
REMARK 500 5 SER A 72 102.48 69.58
REMARK 500 6 SER A 6 177.68 50.71
REMARK 500 6 PRO A 54 49.56 -78.24
REMARK 500 6 ASP A 55 145.80 69.27
REMARK 500 6 GLU A 56 92.02 42.46
REMARK 500 6 GLN A 59 -172.82 45.04
REMARK 500 6 LYS A 64 83.51 35.42
REMARK 500 6 SER A 72 -150.79 53.18
REMARK 500 7 SER A 6 102.57 -59.01
REMARK 500 7 ALA A 33 171.93 -55.28
REMARK 500 7 ASP A 55 -62.69 -167.68
REMARK 500 7 GLU A 56 78.69 30.30
REMARK 500 7 PHE A 61 82.92 -155.52
REMARK 500 7 LEU A 63 58.57 -143.72
REMARK 500 8 SER A 3 -159.19 48.22
REMARK 500 8 ASP A 55 -63.18 -163.40
REMARK 500 8 LYS A 58 68.46 39.30
REMARK 500 8 LYS A 64 68.54 39.08
REMARK 500 8 SER A 71 -98.57 47.47
REMARK 500 8 SER A 72 -39.61 -146.22
REMARK 500
REMARK 500 THIS ENTRY HAS 115 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 2 SER A 3 5 149.98
REMARK 500 PRO A 70 SER A 71 5 -149.55
REMARK 500 GLY A 53 PRO A 54 10 -146.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 3 ARG A 11 0.09 SIDE CHAIN
REMARK 500 3 ARG A 26 0.08 SIDE CHAIN
REMARK 500 6 ARG A 11 0.08 SIDE CHAIN
REMARK 500 6 ARG A 24 0.10 SIDE CHAIN
REMARK 500 10 ARG A 24 0.08 SIDE CHAIN
REMARK 500 16 ARG A 11 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002013898.1 RELATED DB: TARGETDB
DBREF 1X59 A 8 67 UNP P12081 SYH_HUMAN 1 60
SEQADV 1X59 GLY A 1 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 SER A 2 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 SER A 3 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 GLY A 4 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 SER A 5 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 SER A 6 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 GLY A 7 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 SER A 68 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 GLY A 69 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 PRO A 70 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 SER A 71 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 SER A 72 UNP P12081 CLONING ARTIFACT
SEQADV 1X59 GLY A 73 UNP P12081 CLONING ARTIFACT
SEQRES 1 A 73 GLY SER SER GLY SER SER GLY MET ALA GLU ARG ALA ALA
SEQRES 2 A 73 LEU GLU GLU LEU VAL LYS LEU GLN GLY GLU ARG VAL ARG
SEQRES 3 A 73 GLY LEU LYS GLN GLN LYS ALA SER ALA GLU LEU ILE GLU
SEQRES 4 A 73 GLU GLU VAL ALA LYS LEU LEU LYS LEU LYS ALA GLN LEU
SEQRES 5 A 73 GLY PRO ASP GLU SER LYS GLN LYS PHE VAL LEU LYS THR
SEQRES 6 A 73 PRO LYS SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 7 GLN A 31 1 25
HELIX 2 2 SER A 34 GLY A 53 1 20
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes